ID A0A1V0GYS6_9RHOB Unreviewed; 389 AA.
AC A0A1V0GYS6;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Acetate kinase {ECO:0000256|HAMAP-Rule:MF_00020};
DE EC=2.7.2.1 {ECO:0000256|HAMAP-Rule:MF_00020};
DE AltName: Full=Acetokinase {ECO:0000256|HAMAP-Rule:MF_00020};
GN Name=ackA {ECO:0000256|HAMAP-Rule:MF_00020};
GN ORFNames=A6J80_21290 {ECO:0000313|EMBL:ARC38839.1}, H7K23_19035
GN {ECO:0000313|EMBL:MBY0138124.1}, PY32053_04260
GN {ECO:0000313|EMBL:AYF03790.1}, PYTT13_13210
GN {ECO:0000313|EMBL:ATQ56653.1};
OS Paracoccus yeei.
OG Plasmid pYEE3 {ECO:0000313|EMBL:AYF03790.1},
OG Plasmid pyee3 {ECO:0000313|Proteomes:UP000272010}, and
OG Plasmid unnamed4 {ECO:0000313|EMBL:ARC38839.1,
OG ECO:0000313|Proteomes:UP000191257}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=147645 {ECO:0000313|EMBL:ARC38839.1, ECO:0000313|Proteomes:UP000191257};
RN [1] {ECO:0000313|Proteomes:UP000191257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_252 {ECO:0000313|Proteomes:UP000191257};
RC PLASMID=Plasmid unnamed4 {ECO:0000313|Proteomes:UP000191257};
RA Minogue T., Wolcott M., Wasieloski L., Aguilar W., Moore D., Tallon L.,
RA Sadzewicz L., Sengamalay N., Ott S., Godinez A., Nagaraj S., Nadendla S.,
RA Geyer C., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ATQ56653.1, ECO:0000313|Proteomes:UP000229314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TT13 {ECO:0000313|EMBL:ATQ56653.1,
RC ECO:0000313|Proteomes:UP000229314};
RA Lee K., Lim J.Y., Hwang I.;
RT "Complete genome sequence of Paracoccus yeei TT13 isolated from human
RT skin.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:ARC38839.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FDAARGOS_252 {ECO:0000313|EMBL:ARC38839.1};
RC PLASMID=unnamed4 {ECO:0000313|EMBL:ARC38839.1};
RA Campos J., Goldberg B., Tallon L., Sadzewicz L., Sengamalay N., Ott S.,
RA Godinez A., Nagaraj S., Vyas G., Aluvathingal J., Nadendla S., Geyer C.,
RA Nandy P., Hobson J., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AYF03790.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCUG 32053 {ECO:0000313|EMBL:AYF03790.1};
RC PLASMID=pYEE3 {ECO:0000313|EMBL:AYF03790.1};
RX PubMed=30410477; DOI=10.3389/fmicb.2018.02553;
RA Lasek R., Szuplewska M., Mitura M., Decewicz P., Chmielowska C., Pawlot A.,
RA Sentkowska D., Czarnecki J., Bartosik D.;
RT "Genome Structure of the Opportunistic Pathogen Paracoccus yeei
RT (Alphaproteobacteria) and Identification of Putative Virulence Factors.";
RL Front. Microbiol. 9:2553-2553(2018).
RN [5] {ECO:0000313|Proteomes:UP000272010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 32053 {ECO:0000313|Proteomes:UP000272010};
RC PLASMID=pyee3 {ECO:0000313|Proteomes:UP000272010};
RA Lasek R., Szuplewska M., Mitura M., Decewicz P., Chmielowska C., Pawlot A.,
RA Sentkowska D., Czarnecki J., Bartosik D.;
RT "Genome Structure of the Opportunistic Pathogen Paracoccus yeei
RT (Alphaproteobacteria) and Identification of Putative Virulence Factors.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
RN [6] {ECO:0000313|EMBL:MBY0138124.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S/N-202-OC-B2 {ECO:0000313|EMBL:MBY0138124.1};
RA Seuylemezian A., Singh N.K., Wood J., Venkateswaran K.;
RT "Fungal Genomes of the International Space Station.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of acetyl phosphate from acetate and
CC ATP. Can also catalyze the reverse reaction. {ECO:0000256|HAMAP-
CC Rule:MF_00020}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP = acetyl phosphate + ADP; Xref=Rhea:RHEA:11352,
CC ChEBI:CHEBI:22191, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:456216; EC=2.7.2.1; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_00020};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00020};
CC Note=Mg(2+). Can also accept Mn(2+). {ECO:0000256|HAMAP-Rule:MF_00020};
CC -!- PATHWAY: Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis;
CC acetyl-CoA from acetate: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00020}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|HAMAP-Rule:MF_00020}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00020}.
CC -!- SIMILARITY: Belongs to the acetokinase family.
CC {ECO:0000256|ARBA:ARBA00008748, ECO:0000256|HAMAP-Rule:MF_00020,
CC ECO:0000256|RuleBase:RU003835}.
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DR EMBL; CP020444; ARC38839.1; -; Genomic_DNA.
DR EMBL; CP024422; ATQ56653.1; -; Genomic_DNA.
DR EMBL; CP031081; AYF03790.1; -; Genomic_DNA.
DR EMBL; JACLBQ010000080; MBY0138124.1; -; Genomic_DNA.
DR RefSeq; WP_035745643.1; NZ_JACLBQ010000080.1.
DR GeneID; 78898608; -.
DR KEGG; pye:A6J80_21290; -.
DR UniPathway; UPA00340; UER00458.
DR Proteomes; UP000191257; Plasmid unnamed4.
DR Proteomes; UP000229314; Chromosome.
DR Proteomes; UP000272010; Plasmid pyee3.
DR Proteomes; UP000756578; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008776; F:acetate kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00020; Acetate_kinase; 1.
DR InterPro; IPR004372; Ac/propionate_kinase.
DR InterPro; IPR000890; Aliphatic_acid_kin_short-chain.
DR InterPro; IPR023865; Aliphatic_acid_kinase_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR NCBIfam; TIGR00016; ackA; 1.
DR PANTHER; PTHR21060; ACETATE KINASE; 1.
DR PANTHER; PTHR21060:SF15; PROPIONATE KINASE PDUW; 1.
DR Pfam; PF00871; Acetate_kinase; 1.
DR PIRSF; PIRSF000722; Acetate_prop_kin; 1.
DR PRINTS; PR00471; ACETATEKNASE.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS01076; ACETATE_KINASE_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00020};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00020};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00020};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_00020};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00020};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00020}; Plasmid {ECO:0000313|EMBL:ARC38839.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000191257};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00020}.
FT ACT_SITE 148
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 10
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 91
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 203..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 278..280
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 323..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT BINDING 374
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 179
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
FT SITE 236
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00020"
SQ SEQUENCE 389 AA; 41347 MW; D29EC8F50D80A2A5 CRC64;
MTRDLILTFN TGSSTIKLGF YALEAAAPRP LASGVIDFRD EPFEVRLTRE GKTFSGPITA
DPGDLTAVLN QAFAWLAGHF NLSRLAVIGH RVVHGGDVFT GPARITDQVI AQIDALARLA
PLHQPQSLAL IRAMRGLYPD VPQTASFDTA FHATNPPLIR RFALPRALYD QGIKRYGFHG
LSYRYIAGQL GDLATDAKVV AAHLGSGASL CAIRGGKSID SSMGFSTLDG IPMATRSGAL
DPGVILHLMG EMGQSLKQVE TMLYRESGLL GVSGFEADSR ELMASTRPEA AEAIDLFCLR
IAGEVARLAT SMGGIDALVF TAGIGEHQPG IRARVAARLA WLGAELDPDA NEAGSRRIST
AASRVQLLVI PTDEESIIAQ EAVSEEAAT
//
